2VDE

Crystal Structure of the Open State of TolC Outer Membrane Component of Mutlidrug Efflux Pumps

2VDE の概要

• エントリーDOI: 10.2210/pdb2vde/pdb
• 関連するPDBエントリー: 1EK9 1TQQ 1TTQ 2VDD
• 分子名称: OUTER MEMBRANE PROTEIN TOLC, CHLORIDE ION (2 entities in total)
• 機能のキーワード: outer membrane, alpha helical barrel, transport protein, multidrug efflux pump, integral membrane protein, membrane, transport, beta barrel, transmembrane
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 152010.81

構造登録者

Bavro, V.N.,Pietras, Z.,Furnham, N.,Perez-Cano, L.,Fernandez-Recio, J.,Pei, X.Y.,Truer, R.,Misra, R.,Luisi, B. (登録日: 2007-10-04, 公開日: 2008-04-22, 最終更新日: 2023-12-13)

主引用文献

Bavro, V.N.,Pietras, Z.,Furnham, N.,Perez-Cano, L.,Fernandez-Recio, J.,Pei, X.Y.,Truer, R.,Misra, R.,Luisi, B.
Assembly and Channel Opening in a Bacterial Drug Efflux Machine.
Mol.Cell, 30:114-, 2008

PubMed Abstract: Drugs and certain proteins are transported across the membranes of Gram-negative bacteria by energy-activated pumps. The outer membrane component of these pumps is a channel that opens from a sealed resting state during the transport process. We describe two crystal structures of the Escherichia coli outer membrane protein TolC in its partially open state. Opening is accompanied by the exposure of three shallow intraprotomer grooves in the TolC trimer, where our mutagenesis data identify a contact point with the periplasmic component of a drug efflux pump, AcrA. We suggest that the assembly of multidrug efflux pumps is accompanied by induced fit of TolC driven mainly by accommodation of the periplasmic component.

PubMed: 18406332
DOI: 10.1016/J.MOLCEL.2008.02.015

実験手法

X-RAY DIFFRACTION (3.2 Å)